1A6I
TET REPRESSOR, CLASS D VARIANT
Summary for 1A6I
| Entry DOI | 10.2210/pdb1a6i/pdb |
| Descriptor | TETRACYCLINE REPRESSOR PROTEIN CLASS D (2 entities in total) |
| Functional Keywords | transcription regulation, repressor, dna-binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 24319.69 |
| Authors | Orth, P.,Cordes, F.,Schnappinger, D.,Hillen, W.,Saenger, W.,Hinrichs, W. (deposition date: 1998-02-25, release date: 1999-03-02, Last modification date: 2024-05-22) |
| Primary citation | Orth, P.,Cordes, F.,Schnappinger, D.,Hillen, W.,Saenger, W.,Hinrichs, W. Conformational changes of the Tet repressor induced by tetracycline trapping. J.Mol.Biol., 279:439-447, 1998 Cited by PubMed Abstract: The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations. PubMed: 9642048DOI: 10.1006/jmbi.1998.1775 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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